ID   PRS8_NAEFO              Reviewed;         414 AA.
AC   Q25544;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=26S proteasome regulatory subunit 8 homolog;
DE   AltName: Full=Tat-binding protein homolog;
OS   Naegleria fowleri (Brain eating amoeba).
OC   Eukaryota; Discoba; Heterolobosea; Tetramitia; Eutetramitia;
OC   Vahlkampfiidae; Naegleria.
OX   NCBI_TaxID=5763;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=LEE mp;
RA   Sullivan P.K., Shaw D.R., Marciano-Cabral F., Ennis H.L.;
RT   "Isolation and characterization of a Naegleria fowleri Tat-binding protein
RT   cDNA.";
RL   Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The 26S proteasome is involved in the ATP-dependent
CC       degradation of ubiquitinated proteins. The regulatory (or ATPase)
CC       complex confers ATP dependency and substrate specificity to the 26S
CC       complex (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR   EMBL; U41812; AAB01762.1; -; mRNA.
DR   AlphaFoldDB; Q25544; -.
DR   SMR; Q25544; -.
DR   VEuPathDB; AmoebaDB:FDP41_005397; -.
DR   VEuPathDB; AmoebaDB:NF0015020; -.
DR   VEuPathDB; AmoebaDB:NfTy_065890; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0036402; F:proteasome-activating activity; IEA:InterPro.
DR   GO; GO:0030163; P:protein catabolic process; IEA:InterPro.
DR   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR005937; 26S_Psome_P45-like.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR041569; AAA_lid_3.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR032501; Prot_ATP_ID_OB_C.
DR   InterPro; IPR035261; PSMC5.
DR   PANTHER; PTHR23073:SF102; PTHR23073:SF102; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF17862; AAA_lid_3; 1.
DR   Pfam; PF16450; Prot_ATP_ID_OB; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01242; 26Sp45; 1.
DR   PROSITE; PS00674; AAA; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; Nucleotide-binding; Nucleus; Proteasome.
FT   CHAIN           1..414
FT                   /note="26S proteasome regulatory subunit 8 homolog"
FT                   /id="PRO_0000084729"
FT   BINDING         197..204
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   414 AA;  45999 MW;  628D3A2D3B3024C3 CRC64;
     MLNTSTSGGS GVHVVLASSS SASVNGLKNY YIAKIQEKEI VLRDKIENLR RLQAQRNELN
     GRVRSLKEEL QQLQEPGSHV GEVVKVMGKK KVLIKISQEG KYIVDIDKSI ELKDLTPGVR
     VALRNDSYAL HKILPNKIDP LVSLMKVEKV PDATYEMVGG LDEQIKEIKE VIELPIKHPE
     LFESLGIAQP KGVIMYGPPG TGKTLLARAV AHHTDCTFIR VSGSELVQKY IGEGSKMVRE
     LFVMAREHAP SIIFMDEIDS IGSTRTEGGK GGGDSEVQRT MLELLNQLDG FESTQNIKII
     MATNRIDILD PALLRPGRID RKIEFPNPNE LARLDILKIH SRRMNLTRGI NLRKIASMLG
     GASGAEIKAT CTEAGMFALR ERRVHVTQED LEMAVAKVMK RGDESNMSFK KLFK